A terminal 6-sulfotransferase catalyzing a synthesis of N-acetylgalactosamine 4,6-bissulfate residue at the nonreducing terminal position of chondroitin sulfate.
A soluble enzyme from quail oviduct which incorporates sulfate into position 6 of the nonreducing N-acetylgalactosamine 4-sulfate end group of chondroitin sulfate has been purified. This enzyme (termed "terminal 6-sulfotransferase") was partially separated from a 6-sulfotransferase present in the same tissue which catalyzes the incorporation of sulfate into interior portion of unsulfated chondroitin. The basic requirements for the terminal 6-sulfotransferase reaction were shown to be 3'-phosphoadenylyl sulfate (donor) and chondroitin 4-sulfate (acceptor). The substitution of unsulfated chondroitin (prepared from squid skin) for chondroitin 4-sulfate resulted in a total loss of activity. These results suggest that the organization of the proteoglycan-synthesizing apparatus may well involve hitherto unrecognized mechanisms for the sulfation of chondroitin chains.
D000116:Acetylgalactosamine / Q000031:analogs & derivatives* / Q000138:chemical synthesis; D000818:Animals; D002240:Carbohydrate Sequence; D002807:Chondroitin / Q000031:analogs & derivatives*; D002809:Chondroitin Sulfates / Q000096:biosynthesis*; D005260:Female; D005688:Galactosamine / Q000031:analogs & derivatives*; D010057:Oviducts / Q000201:enzymology*; D011784:Quail; D013466:Sulfurtransferases / Q000302:isolation & purification / Q000378:metabolism*
C030330:N-acetylgalactosamine 4,6-bisulfate; D005688:Galactosamine; D002807:Chondroitin; D002809:Chondroitin Sulfates; D013466:Sulfurtransferases; D000116:Acetylgalactosamine